2. Academic Validation
  3. ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells

ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells

  • FEBS Lett. 1999 May 14;451(1):81-4. doi: 10.1016/s0014-5793(99)00550-5.
M Murata-Hori 1,  F Suizu,  T Iwasaki,  A Kikuchi,  H Hosoya
Affiliations

Affiliation

  • 1 Department of Biological Science, Faculty of Science, Hiroshima University, Higashi-Hiroshima, Japan.
PMID: 10356987 DOI: 10.1016/s0014-5793(99)00550-5
Abstract

A novel Myosin light chain kinase (MLCK) cDNA was isolated from a HeLa cell cDNA library. The deduced amino acid sequence was identical to that of a zipper-interacting protein kinase (ZIPK) which mediates Apoptosis [Kawai et al. (1998) Mol. Cell. Biol. 18, 1642-1651]. Here we found that HeLa ZIPK phosphorylated the regulatory LIGHT chain of Myosin II (MRLC) at both serine 19 and threonine 18 in a Ca2+/Calmodulin independent manner. Phosphorylation of Myosin II by HeLa ZIPK resulted in activation of actin-activated MgATPase activity of Myosin II. HeLa ZIPK is the first non-muscle MLCK that phosphorylates MRLC at two sites.

Figures